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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1992-6-22
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pubmed:abstractText |
A survey of protein-protein interactions in structures derived by X-ray crystallography of protease-inhibitor and antigen-antibody complexes shows that they form close-packed interfaces from which water is excluded. The interfaces are of almost constant size, and they contain about ten hydrogen bonds. These features account for the stability of the complexes. To test whether they also account for specificity, we designed a computer simulation that searches for complementary surfaces on two protein molecules. In all cases tested, the simulation finds a number of complexes having interfaces and hydrogen bonds equivalent to those of the native complexes. These artificial complexes might represent secondary specificities, which can be detected when normal association is prevented by mutation or other means.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0300-5208
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
161
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
237-49; discussion 250-2
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pubmed:dateRevised |
2000-12-18
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pubmed:meshHeading |
pubmed-meshheading:1814694-Computer Simulation,
pubmed-meshheading:1814694-Crystallography,
pubmed-meshheading:1814694-Models, Chemical,
pubmed-meshheading:1814694-Models, Molecular,
pubmed-meshheading:1814694-Protein Conformation,
pubmed-meshheading:1814694-Protein Denaturation,
pubmed-meshheading:1814694-Proteins,
pubmed-meshheading:1814694-Surface Properties
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pubmed:year |
1991
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pubmed:articleTitle |
Protein-protein interaction: an analysis by computer simulation.
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pubmed:affiliation |
Laboratoire de Biologie Physicochimique, UA 1131 CNRS, Université Paris-Sud, Orsay, France.
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pubmed:publicationType |
Journal Article
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